Strong Ligand-Protein Interactions Derived from Diffuse Ligand Interactions with Loose Binding Sites

Strong Ligand-Protein Interactions Derived from Diffuse Ligand Interactions with Loose Binding Sites

Many systems in biology rely on binding of ligands to target proteins in a single high-affinity conformation with a favorable ΔG. Alternatively, interactions of ligands with protein regions that allow diffuse binding, distributed over multiple sites and conformations, can exhibit favorable ΔG because of their higher entropy. Diffuse binding may be biologically important for multidrug transporte...

Protein Ligand Interactions 


A - ligand interactions : ( I ) magnesium binding sites in yeast tRNA

X-ray crystallographic studies indicate that there are at least four site-specifically bound hydrated Mg 2 + ions, [Mg(H20)n] , in yeast tRNA. The size and the octahedral coordination geometry, rather than the charge, of [Mg(H2O)n] 2+ appear to be the primary reasons for the specificity of magnesium ions in site-binding and in the stabilization of the tertiary structure of tRNA.

L-usnate-urease interactions: binding sites for the ligand.

L-usnic acid inactivates urease by formation of high molecular weight aggregates which can reached by a maximum of 880 000. L-cysteine partially reverses the inactivation of stimulating the appearance of active high molecular weight polymers. The existence of two class of binding points for L-usnic acid on the urease molecule is proposed, the first showing high affinity for the ligand, related ...

Carbene footprinting accurately maps binding sites in protein–ligand and protein–protein interactions

Specific interactions between proteins and their binding partners are fundamental to life processes. The ability to detect protein complexes, and map their sites of binding, is crucial to understanding basic biology at the molecular level. Methods that employ sensitive analytical techniques such as mass spectrometry have the potential to provide valuable insights with very little material and o...